title: Protein structures, folds and fold spaces.
abstract: There has been considerable progress towards the goal of understanding the space of possible tertiary structures adopted by proteins. Despite a greatly increased rate of structure determination and a deliberate strategy of sequencing proteins expected to be very different from those already known, it is now rare to see a genuinely new fold, leading to the conclusion that we have seen the majority of natural structural types. The increase in knowledge has also led to a critical examination of traditional fold-based classifications and their meaning for evolution and protein structures. We review these issues and discuss possible solutions.
authors.affiliation: Division of Mathematical Biology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
authors.forename: Michael I
authors.initials: MI
authors.lastname: Sadowski
authors.forename: William R
authors.initials: WR
authors.lastname: Taylor
mesh_terms: D000818:Animals; D001703:Biophysics / Q000379:methods*; D002384:Catalysis; D004330:Drosophila; D004926:Escherichia coli / Q000378:metabolism; D007136:Immunoglobulins / Q000737:chemistry; D051379:Mice; D008968:Molecular Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016963:Thermus thermophilus / Q000378:metabolism
chemical_list: D007136:Immunoglobulins; D011506:Proteins